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Database: UniProt
Entry: A0A0F8XBG9_9EURO
LinkDB: A0A0F8XBG9_9EURO
Original site: A0A0F8XBG9_9EURO 
ID   A0A0F8XBG9_9EURO        Unreviewed;       434 AA.
AC   A0A0F8XBG9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=RNA polymerase II Elongator complex associated protein Kti12 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ARAM_006422 {ECO:0000313|EMBL:KKK20962.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK20962.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK20962.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK20962.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT   Species Obtained from the Cote d'Ivoire.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the KTI12 family.
CC       {ECO:0000256|ARBA:ARBA00025768}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKK20962.1}.
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DR   EMBL; JZBS01001898; KKK20962.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8XBG9; -.
DR   STRING; 308745.A0A0F8XBG9; -.
DR   OrthoDB; 375350at2759; -.
DR   Proteomes; UP000034291; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR013641; KTI12/PSTK.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12435:SF2; PROTEIN KTI12 HOMOLOG; 1.
DR   PANTHER; PTHR12435; UNCHARACTERIZED; 1.
DR   Pfam; PF08433; KTI12; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034291}.
FT   REGION          137..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          257..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..274
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   434 AA;  47135 MW;  6BEE434A770B57A2 CRC64;
     MPLIVLTGYP CSGLSYRARQ LASQLENTQN ELFASGAIPS SKPRYKIHIV PTHDVSHPRT
     VYDTARTEKE TRGVAYTRAK RALGRDSFVI LDGMNYIKGY RYQLWCEAKA LGTSCCVVHV
     GTPIDQCVAN NEARLRRKNP HSQELESAQQ SAKEESVSES QTCPTPPPPP KEEDTEDPYP
     PELLNNLIFR YEEPNIHSRW DKPLFTVPWS DVEPPIAEIW TALTGLPHPS TLSQTDQAPD
     DASSISTLAA ALSLTSPTNL SSAASTTTAA PSGTRAAALQ RPRIKPHQAT VLPTATASSA
     LYNIEKRTSA IVQAIRSFSL SNPSAKAALA QSQSAKVRTR PGEEGITIVV PEASIPIFIP
     VHIASASTTD DLAAAGGILA LPRLQRLRRQ WIALNRAYVA GPHASGKGGL MDDQIADAFV
     RFLNADFADE VDER
//
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